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MA6D1_MOUSE
ID   MA6D1_MOUSE             Reviewed;         191 AA.
AC   Q14BB9; Q3TQE2; Q8C540;
DT   09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   22-AUG-2006, sequence version 1.
DT   03-AUG-2022, entry version 100.
DE   RecName: Full=MAP6 domain-containing protein 1;
DE   AltName: Full=21 kDa STOP-like protein;
DE            Short=SL21;
GN   Name=Map6d1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Medulla oblongata, and Spinal cord;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND INTERACTION WITH CALMODULIN.
RX   PubMed=16837464; DOI=10.1074/jbc.m603380200;
RA   Gory-Faure S., Windscheid V., Bosc C., Peris L., Proietto D., Franck R.,
RA   Denarier E., Job D., Andrieux A.;
RT   "STOP-like protein 21 is a novel member of the STOP family, revealing a
RT   Golgi localization of STOP proteins.";
RL   J. Biol. Chem. 281:28387-28396(2006).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-38; SER-41 AND SER-160, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
CC   -!- FUNCTION: May have microtubule-stabilizing activity.
CC   -!- SUBUNIT: Interacts with calmodulin. {ECO:0000269|PubMed:16837464}.
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus {ECO:0000269|PubMed:16837464}.
CC       Cytoplasm, cytoskeleton {ECO:0000269|PubMed:16837464}. Note=According
CC       to PubMed:16837464, it colocalizes with microtubules.
CC   -!- TISSUE SPECIFICITY: Expressed in brain. Found in neurons in primary
CC       cultures, but absent in glial cells. {ECO:0000269|PubMed:16837464}.
CC   -!- PTM: Palmitoylated. Palmitoylation enhances association with
CC       microtubules (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the STOP family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC37698.1; Type=Frameshift; Evidence={ECO:0000305};
CC       Sequence=BAE37442.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=BAE37442.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; AK163656; BAE37442.1; ALT_INIT; mRNA.
DR   EMBL; AK079603; BAC37698.1; ALT_FRAME; mRNA.
DR   EMBL; BC116220; AAI16221.1; -; mRNA.
DR   EMBL; BC116221; AAI16222.1; -; mRNA.
DR   CCDS; CCDS37286.1; -.
DR   RefSeq; NP_941001.2; NM_198599.2.
DR   AlphaFoldDB; Q14BB9; -.
DR   BioGRID; 228955; 2.
DR   IntAct; Q14BB9; 1.
DR   MINT; Q14BB9; -.
DR   STRING; 10090.ENSMUSP00000043332; -.
DR   iPTMnet; Q14BB9; -.
DR   PhosphoSitePlus; Q14BB9; -.
DR   SwissPalm; Q14BB9; -.
DR   MaxQB; Q14BB9; -.
DR   PaxDb; Q14BB9; -.
DR   PeptideAtlas; Q14BB9; -.
DR   PRIDE; Q14BB9; -.
DR   ProteomicsDB; 252708; -.
DR   Antibodypedia; 50914; 18 antibodies from 10 providers.
DR   DNASU; 208158; -.
DR   Ensembl; ENSMUST00000040880; ENSMUSP00000043332; ENSMUSG00000041205.
DR   GeneID; 208158; -.
DR   KEGG; mmu:208158; -.
DR   UCSC; uc007ypk.1; mouse.
DR   CTD; 79929; -.
DR   MGI; MGI:3607784; Map6d1.
DR   VEuPathDB; HostDB:ENSMUSG00000041205; -.
DR   eggNOG; ENOG502RXB9; Eukaryota.
DR   GeneTree; ENSGT00530000063947; -.
DR   HOGENOM; CLU_089524_0_0_1; -.
DR   InParanoid; Q14BB9; -.
DR   OMA; PREDYQP; -.
DR   OrthoDB; 1408472at2759; -.
DR   PhylomeDB; Q14BB9; -.
DR   TreeFam; TF338320; -.
DR   BioGRID-ORCS; 208158; 1 hit in 74 CRISPR screens.
DR   PRO; PR:Q14BB9; -.
DR   Proteomes; UP000000589; Chromosome 16.
DR   RNAct; Q14BB9; protein.
DR   Bgee; ENSMUSG00000041205; Expressed in lumbar subsegment of spinal cord and 75 other tissues.
DR   Genevisible; Q14BB9; MM.
DR   GO; GO:0005801; C:cis-Golgi network; IDA:MGI.
DR   GO; GO:0005798; C:Golgi-associated vesicle; IDA:MGI.
DR   GO; GO:0005874; C:microtubule; IBA:GO_Central.
DR   GO; GO:0005516; F:calmodulin binding; IDA:MGI.
DR   GO; GO:0008017; F:microtubule binding; IDA:MGI.
DR   GO; GO:0030705; P:cytoskeleton-dependent intracellular transport; IBA:GO_Central.
DR   GO; GO:0000226; P:microtubule cytoskeleton organization; IEA:InterPro.
DR   GO; GO:0018009; P:N-terminal peptidyl-L-cysteine N-palmitoylation; IDA:MGI.
DR   GO; GO:0007026; P:negative regulation of microtubule depolymerization; IDA:MGI.
DR   GO; GO:0070507; P:regulation of microtubule cytoskeleton organization; IBA:GO_Central.
DR   InterPro; IPR007882; MAP6.
DR   PANTHER; PTHR14759; PTHR14759; 1.
PE   1: Evidence at protein level;
KW   Calmodulin-binding; Cytoplasm; Cytoskeleton; Golgi apparatus; Lipoprotein;
KW   Palmitate; Phosphoprotein; Reference proteome.
FT   CHAIN           1..191
FT                   /note="MAP6 domain-containing protein 1"
FT                   /id="PRO_0000271916"
FT   REGION          31..106
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         38
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         41
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         160
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   LIPID           5
FT                   /note="S-palmitoyl cysteine"
FT                   /evidence="ECO:0000250"
FT   LIPID           10
FT                   /note="S-palmitoyl cysteine"
FT                   /evidence="ECO:0000250"
FT   LIPID           11
FT                   /note="S-palmitoyl cysteine"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        24
FT                   /note="V -> F (in Ref. 1; BAC37698)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   191 AA;  20433 MW;  4B1186314324BD3A CRC64;
     MAWPCISRLC CLARRWNQLD RSDVAVPLTL HGYSDPGSEE SGADCSVSRG NPSVAGARES
     SRAVPLTQYQ RDFGVRTARA GSRDAAQERP SGPGGRRGQS SAPPTRTVYV LPVGDADAAV
     VATTSYRQEF QAWTGVKPSR STKARTARVV TTHSSGWDPS PGASFQVPEV RKFTPNPSAI
     FQTSAPQTLN V
 
 
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